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Crystal structure of human tankyrase 2 in complex with ta-92

Analyse Crystal structure of human tankyrase 2 in complex with ta-92 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FPG
Type: protein
Length: 410 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tankyrase-2
UniProt: Q9H2K2
Ligands: Q28, ZN
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 24% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tankyrase-2	protein	205	24% helix, 30% strand	Q9H2K2

Ligands and binding sites

Q28 · 4-[3-(8-methyl-4-oxo-3,4-dihydroquinazolin-2- yl)propanamido]-N-(quinolin-8-yl)benzamide · ligand · 2 copies · chains A, B
ZN · Zinc ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	387	0.74	0.85	40	empty
2	313	0.68	0.82	40	Q28
3	282	0.66	0.82	40	Q28

Interfaces

1 interface between chains.

A–B · 377 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5FPG · Crystal structure of human tankyrase 2 in complex with TA-92 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9H2K2
Elsewhere: RCSB PDB 5FPG · PDBe 5FPG · UniProt Q9H2K2

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